Improved Catalytic Performance of a 2-Haloacid Dehalogenase from Azotobacter sp. by Ion-Exchange Immobilisation

• Published in: Biochemical and biophysical research communications Vol. 220; no. 3; pp. 828 - 833
• Main Authors: Diez, A., Prieto, M.I., Alvarez, M.J., Bautista, J.M., Garrido, A., Puyet, A.
• Format: Journal Article
• Language: English
• Published: United States Elsevier Inc 27-03-1996
• Subjects: Azotobacter; Azotobacter - enzymology; binding; biological treatment; Catalysis; catalytic activity; chemical reactions; DEAE-Cellulose; dechlorination; Enzyme Stability; Enzymes, Immobilized - metabolism; herbicides; Hot Temperature; Hydrogen-Ion Concentration; hydrolases; Hydrolases - isolation & purification; Hydrolases - metabolism; immobilization; Ion Exchange Resins; Kinetics; l-2-haloalkanoic dehalogenase; monochloracetic acid; stability; substrates; temperature; Thermodynamics
• ISSN: 0006-291X; 1090-2104
• DOI: 10.1006/bbrc.1996.0489

The stability and catalytic efficacy of the L-2-haloacid dehalogenase isolated from
Azotobacter sp. RC26 were studied after immobilisation on a DEAE-Sephacel solid matrix. While the optimum temperature for the soluble dehalogenase falls in the range of 30–40°C, the activity of the immobilised enzyme shows a four-fold increase at 60°C. Immobilisation on a plug-flow bioreactor extends the range of usable substrate concentration. The improved catalytic characteristics after immobilisation of the haloacid dehalogenase may be relevant for its possible utilization in biotechnological applications ranging from waste treatment to synthesis of steroiso-mers.